Calcium in PDB 7jnd: The Structure of CBM32-1 and CBM32-2 Domains From Clostridium Perfringens Zmpb

The structure of The Structure of CBM32-1 and CBM32-2 Domains From Clostridium Perfringens Zmpb, PDB code: 7jnd was solved by B.Pluvinage, A.B.Boraston, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.16 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.26, 81.97, 132.53, 90, 90, 90
R / Rfree (%)	23.5 / 27.9

The binding sites of Calcium atom in the The Structure of CBM32-1 and CBM32-2 Domains From Clostridium Perfringens Zmpb (pdb code 7jnd). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the The Structure of CBM32-1 and CBM32-2 Domains From Clostridium Perfringens Zmpb, PDB code: 7jnd:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the The Structure of CBM32-1 and CBM32-2 Domains From Clostridium Perfringens Zmpb


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Structure of CBM32-1 and CBM32-2 Domains From Clostridium Perfringens Zmpb within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca501 b:22.5 occ:1.00 OE2 A:GLU205 2.2 23.4 1.0 O A:ALA204 2.3 30.2 1.0 O A:ASN98 2.3 28.1 1.0 O A:THR101 2.4 25.0 1.0 O A:LYS93 2.4 29.1 1.0 OD1 A:ASP96 2.5 25.0 1.0 OG1 A:THR101 2.6 24.6 1.0 CD A:GLU205 3.3 24.6 1.0 C A:THR101 3.4 27.8 1.0 CG A:ASP96 3.5 24.2 1.0 C A:ASN98 3.5 27.8 1.0 C A:ALA204 3.5 29.5 1.0 C A:LYS93 3.6 26.8 1.0 CG A:GLU205 3.7 26.6 1.0 CB A:THR101 3.8 25.0 1.0 OD2 A:ASP96 3.9 22.3 1.0 CA A:THR101 4.0 25.8 1.0 N A:ASN98 4.0 25.9 1.0 N A:THR101 4.1 29.9 1.0 CA A:ASN98 4.2 28.0 1.0 N A:HIS102 4.3 26.8 1.0 OE1 A:GLU205 4.4 25.6 1.0 CA A:ALA204 4.4 28.3 1.0 CA A:LYS93 4.4 27.6 1.0 N A:GLU205 4.4 27.3 1.0 N A:ASP96 4.4 23.5 1.0 N A:LEU99 4.5 25.5 1.0 N A:ALA94 4.5 26.2 1.0 CA A:GLU205 4.5 25.7 1.0 CA A:ALA94 4.6 24.4 1.0 CA A:HIS102 4.6 27.1 1.0 C A:ALA94 4.6 24.0 1.0 CB A:ASP96 4.7 24.6 1.0 CA A:LEU99 4.7 27.6 1.0 CB A:GLU205 4.7 25.4 1.0 CB A:LYS93 4.7 29.4 1.0 CB A:ASN98 4.7 27.1 1.0 C A:LEU99 4.8 29.6 1.0 N A:GLY97 4.8 29.5 1.0 N A:ILE95 4.8 25.0 1.0 CA A:ASP96 4.9 25.7 1.0 O A:ALA94 4.9 28.5 1.0 CG2 A:THR101 5.0 22.2 1.0 O A:ALA203 5.0 25.1 1.0

Calcium binding site 2 out of 2 in the The Structure of CBM32-1 and CBM32-2 Domains From Clostridium Perfringens Zmpb


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The Structure of CBM32-1 and CBM32-2 Domains From Clostridium Perfringens Zmpb within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca502 b:21.7 occ:1.00 O A:LYS318 2.2 24.8 1.0 O A:ASP323 2.4 24.4 1.0 O A:THR326 2.4 21.3 1.0 OE2 A:GLU427 2.4 23.8 1.0 OD1 A:ASP321 2.4 30.4 1.0 O A:ASN426 2.4 21.4 1.0 OG1 A:THR326 2.5 16.3 1.0 C A:THR326 3.2 22.0 1.0 CG A:ASP321 3.4 28.7 1.0 C A:LYS318 3.5 23.1 1.0 CD A:GLU427 3.5 24.0 1.0 C A:ASP323 3.5 26.9 1.0 C A:ASN426 3.5 19.3 1.0 OD2 A:ASP321 3.7 29.5 1.0 CB A:THR326 3.8 19.4 1.0 CA A:THR326 3.8 19.4 1.0 N A:THR326 3.9 19.7 1.0 N A:ASP323 4.0 28.6 1.0 CG A:GLU427 4.0 23.5 1.0 CA A:ASP323 4.1 28.2 1.0 N A:TYR327 4.2 21.2 1.0 CA A:ASN426 4.3 19.7 1.0 N A:ALA319 4.3 21.6 1.0 CA A:ALA319 4.4 23.5 1.0 N A:ASP321 4.4 28.3 1.0 CB A:ASP323 4.4 30.1 1.0 CA A:LYS318 4.4 22.4 1.0 C A:ALA319 4.4 22.2 1.0 N A:GLU427 4.5 20.6 1.0 OE1 A:GLU427 4.5 23.2 1.0 CA A:TYR327 4.6 20.5 1.0 N A:VAL324 4.6 25.0 1.0 CB A:ASP321 4.6 26.4 1.0 CB A:LYS318 4.7 23.2 1.0 N A:ILE320 4.7 23.8 1.0 CA A:GLU427 4.7 21.0 1.0 O A:ALA319 4.8 22.2 1.0 CG2 A:THR326 4.8 17.0 1.0 N A:ASN322 4.8 28.9 1.0 CA A:VAL324 4.8 25.2 1.0 CA A:ASP321 4.9 27.7 1.0 CB A:ASN426 4.9 18.9 1.0 C A:ASP321 4.9 28.3 1.0 C A:VAL324 4.9 24.4 1.0 N A:ASN325 5.0 22.6 1.0 CB A:GLU427 5.0 24.0 1.0

B.Pluvinage, E.Ficko-Blean, I.Noach, C.Stuart, N.Thompson, H.Mcclure, N.Buenbrazo, W.Wakarchuck, A.B.Boraston. Molecular Insights Into Architecturally Complex Glycopeptidases To Be Published.